Evidence map›Paper›PMID 20368455›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Three-dimensional distribution of transient interactions in the nuclear pore complex obtained from single-molecule snapshots.

Jiong Ma, Weidong Yang

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
4.9field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

77 citing papers in PubMed, 122 citations in OpenAlex.

  1. Review
  2. O-GlcNAc modulation of nuclear pore complexes orchestrates mRNA export efficiency.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Review
  12. Review
  13. Review
  14. Unraveling docking and initiation of mRNA export through the nuclear pore complex.BioEssays : news and reviews in molecular, cellular and developmental biology · 2022
    Article
  15. Article
  16. Article
  17. Imaging Organization of RNA Processing within the Nucleus.Cold Spring Harbor perspectives in biology · 2021
    Review
  18. Review
  19. Article
  20. Article

17 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Jiong MaDepartment of Biological Sciences, Center for Photochemical Sciences, Bowling Green State University, Bowling Green, OH 43403, USA.
Weidong Yang
Bowling Green State University · US

Funding

Three-Dimensional Super-Resolution Microscopy Study of Nuclear TransportR01GM097037 · NIGMS · TEMPLE UNIV OF THE COMMONWEALTH · PI YANG, WEIDONG · 2011 to 2015
$1.3M
NIGMS NIH HHS R01 GM097037
6 · The paper itself

Abstract

The translocation of large macromolecules through the nuclear pore complex (NPC) of eukaryotic cells is hindered by the phenylalanine-glycine (FG) nucleoporin (Nup) barrier unless molecules are chaperoned by transport receptors. The precise mechanism of facilitated translocation remains unclear due to the challenges of measuring the series of transient interactions between a transport receptor and the FG-Nups. This study developed single-point edge-excitation subdiffraction microscopy to obtain a three-dimensional density map of the transient interactions with a spatiotemporal resolution of 9 nm and 400 mus. Three unique features were observed under real-time trafficking conditions that have escaped detection by conventional electron microscopy: (i) the spatial density of interaction sites between Importin beta1 (Imp beta1, a major transport receptor) and the FG-Nups gradually increases from both sides of the NPC and is highest in the central pore region; (ii) cargo-free or cargo-bound Imp beta1 rarely occupies an axial channel with a diameter of approximately 10-20 nm at its narrowest point through the NPC; and (iii) the pathway of facilitated translocation through the NPC depends more on the interaction sites of the FG-Nups than on the NPC architecture.

Indexed as

beta KaryopherinsGlycineGreen Fluorescent ProteinsHeLa CellsHumansImaging, Three-DimensionalMicroscopyNuclear PoreNuclear Pore Complex ProteinsOptics and PhotonicsPhenylalanineProtein ConformationProtein TransportRNATime Factorsbeta KaryopherinsGlycineGreen Fluorescent ProteinsKPNB1 protein, humanNuclear Pore Complex ProteinsPhenylalanineRNA

Identifiers

PMID20368455
PMCPMC2867735
OpenAlexW2031620243

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.